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. 1985 Jun;82(11):3582–3585. doi: 10.1073/pnas.82.11.3582

Three-dimensional structure of ubiquitin at 2.8 A resolution.

S Vijay-Kumar, C E Bugg, K D Wilkinson, W J Cook
PMCID: PMC397829  PMID: 2987935

Abstract

The three-dimensional structure of ubiquitin has been determined at 2.8 A resolution. X-ray diffraction data for the native protein and derivatives were collected with an automated diffractometer. Phases were obtained by use of a single isomorphous mercuric acetate derivative. The molecule contains a pronounced hydrophobic core. Prominent secondary structural features include three and one-half turns of alpha-helix, a mixed beta-sheet that contains four strands, and seven reverse turns. The histidine, tyrosine, and two phenylalanine residues are located on the surface of the molecule.

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Selected References

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